New protein design research could deter chemical, biological attacks
Proteins use transition states to stabilize high-energy substrate conformations in order to obtain catalysis, an acceleration of a chemical reaction with the use of catalyst material. The research project led by Ilya Elashvili of DTRA's Chemical and Biological Technologies Department, David Baker of the University of Washington and Peter Schultz of the Scripps Research Institute has reported a method to prolong this state of transition. Normally transition states in proteins last under one-billionth of a second.
The team members detailed their methodology in "Trapping a Transition State in a Computationally Designed Protein Bottle," an article published by Science. Their methods involved the use of biphenylalanine, a non-canonical amino acid.
They state that if the team is able to redesign a candidate protein to be a highly complementary model for the amino acid, it could allow for the design capabilities to create proteins that would be able to neutralize harmful agents. One possible outcome of this research, according to researchers, could potentially allow military, defense and response personnel to release proteins to neutralize harmful chemical or biological agents in the air.